Evidence map›Paper›PMID 27667502›Full record

ArticleMolecular microbiology2016

ClpAP is an auxiliary protease for DnaA degradation in Caulobacter crescentus.

Jing Liu, Laura I Francis, Kristina Jonas, Michael T Laub, Peter Chien

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. How Rhizobia Adapt to the Nodule Environment.Journal of bacteriology · 2021
    Article
  13. Energy Starvation Induces a Cell Cycle Arrest inFrontiers in molecular biosciences · 2021
    Article
  14. The Protein Quality Control Network inFrontiers in molecular biosciences · 2021
    Review
  15. Article
  16. Review
  17. Multilayered control of chromosome replication inBiochemical Society transactions · 2019
    Review
  18. Article
  19. Reduction in adaptor amounts establishes degradation hierarchy among protease substrates.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Jing LiuMolecular and Cellular Biology Graduate Program, Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA, USA.
Laura I FrancisDepartment of Biology, University of Massachusetts Amherst, Amherst, MA, USA.
Kristina JonasHoward Hughes Medical Institute and Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Michael T LaubHoward Hughes Medical Institute and Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Peter ChienMolecular and Cellular Biology Graduate Program, Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA, USA.
Amherst College · USHoward Hughes Medical Institute · USMassachusetts Institute of Technology · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Cell Cycle Regulation in Caulobacter CrescentusR01GM082899 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LAUB, MICHAEL · 2008 to 2020
$3.8M
Stress related proteases in Caulobacter crescentusR01GM111706 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHIEN, PETER · 2014 to 2018
$1.6M
NIGMS NIH HHS R01 GM082899NIGMS NIH HHS R01 GM111706NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

The Clp family of proteases is responsible for controlling both stress responses and normal growth. In Caulobacter crescentus, the ClpXP protease is essential and drives cell cycle progression through adaptor-mediated degradation. By contrast, the physiological role for the ClpAP protease is less well understood with only minor growth defects previously reported for ΔclpA cells. Here, we show that ClpAP plays an important role in controlling chromosome content and cell fitness during extended growth. Cells lacking ClpA accumulate aberrant numbers of chromosomes upon prolonged growth suggesting a defect in replication control. Levels of the replication initiator DnaA are elevated in ΔclpA cells and degradation of DnaA is more rapid in cells lacking the ClpA inhibitor ClpS. Consistent with this observation, ClpAP degrades DnaA in vitro while ClpS inhibits this degradation. In cells lacking Lon, the protease previously shown to degrade DnaA in Caulobacter, ClpA overexpression rescues defects in fitness and restores degradation of DnaA. Finally, we show that cells lacking ClpA are particularly sensitive to inappropriate increases in DnaA activity. Our work demonstrates an unexpected effect of ClpAP in directly regulating replication through degradation of DnaA and expands the functional role of ClpAP in Caulobacter.

Indexed as

Bacterial ProteinsCaulobacterCaulobacter crescentusCell DivisionChromosomes, BacterialDNA-Binding ProteinsDNA ReplicationEndopeptidase ClpPeptide HydrolasesBacterial ProteinsDnaA protein, BacteriaDNA-Binding ProteinsEndopeptidase ClpPeptide Hydrolases

Identifiers

PMID27667502
PMCPMC5161677
OpenAlexW2526595556

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.